Evidence map›Paper›PMID 22678432›Full record

ArticleNature protocols2012

Determination of site-specific glycan heterogeneity on glycoproteins.

Daniel Kolarich, Pia H Jensen, Friedrich Altmann, Nicolle H Packer

Abstract read
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In one paragraph

Article in Nature protocols, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
9.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

81 citing papers in PubMed, 191 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Glycosylation and the global virome.Molecular ecology · 2023
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021
    Review
  14. The Hitchhiker's guide to glycoproteomics.Biochemical Society transactions · 2021
    Review
  15. Review
  16. Article
  17. Review
  18. Optimal Dissociation Methods Differ forJournal of proteome research · 2020
    Article
  19. Stable Protein Sialylation in Physcomitrella.Frontiers in plant science · 2020
    Article
  20. Review

21 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 3 countries.

Daniel KolarichBiomolecular Frontiers Research Centre, Faculty of Science, Macquarie University, Sydney, New South Wales, Australia.
Pia H Jensen
Friedrich Altmann
Nicolle H Packer
Max Planck Society · DEBOKU University · ATMacquarie University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics. This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG). Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS). If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed. Particular emphasis is placed on data interpretation and the determination of site-specific glycan heterogeneity. The described workflow takes approximately 3-5 d, including sample preparation and data analysis. The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.

Indexed as

Chromatography, LiquidElectrophoresis, Polyacrylamide GelErythropoietinGlycoproteinsGlycosylationHumansPolysaccharidesProteomicsSoftwareTandem Mass SpectrometryEPO protein, humanErythropoietinGlycoproteinsPolysaccharides

Identifiers

PMID22678432
OpenAlexW2080105457

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.